Increases in fragmented glial fibrillary acidic protein levels in the spinal cords of patients with amyotrophic lateral sclerosis.
Using one-dimensional polyacrylamide gel electrophoresis, we analyzed protein fractions extracted from the spinal cords of patients with amyotrophic lateral sclerosis (ALS). Several protein bands with molecular weights of 35-55 kDa were stained with Coomassie brilliant blue much more intensely in the ALS than in the non-ALS spinal cord. Glial fibrillary acidic protein (GFAP) immunoreactivity showed a significant decrease of 50 and 45 kDa band and increase in fragmented 36 and 37 kDa bands, which represented GFAP fragments devoid of 59 and 40 residues from the N-terminal, respectively, as determined by protein sequence analysis. Immunohistochemical examination of ALS spinal cord transections demonstrated increased GFAP-stained astrocytes in the shrunken ventral horn with massive degeneration of motoneurons. These results will provide new insight into the possible role of astrocytes in the pathophysiology and/or pathogenesis of ALS.
Fujita
K
K
Department of Physiology, School of Medicine, Fujita Health University, Toyoake, Aichi, Japan.
Kato
T
T
Yamauchi
M
M
Ando
M
M
Honda
M
M
Nagata
Y
Y
D000595:Amino Acid Sequence; D000690:Amyotrophic Lateral Sclerosis / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005904:Glial Fibrillary Acidic Protein / Q000737:chemistry / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D007150:Immunohistochemistry; D007202:Indicators and Reagents; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012394:Rosaniline Dyes; D013116:Spinal Cord / Q000737:chemistry / Q000378:metabolism*
D005904:Glial Fibrillary Acidic Protein; D007202:Indicators and Reagents; D012394:Rosaniline Dyes; C004692:coomassie Brilliant Blue